1B74
GLUTAMATE RACEMASE FROM AQUIFEX PYROPHILUS
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0008360 | biological_process | regulation of cell shape |
| A | 0008881 | molecular_function | glutamate racemase activity |
| A | 0009252 | biological_process | peptidoglycan biosynthetic process |
| A | 0016853 | molecular_function | isomerase activity |
| A | 0016855 | molecular_function | racemase and epimerase activity, acting on amino acids and derivatives |
| A | 0047661 | molecular_function | amino-acid racemase activity |
| A | 0071555 | biological_process | cell wall organization |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE DGN A 538 |
| Chain | Residue |
| A | ALA69 |
| A | CYS70 |
| A | ASN71 |
| A | GLU147 |
| A | GLY177 |
| A | CYS178 |
| A | HOH540 |
| A | HOH599 |
Functional Information from PROSITE/UniProt
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | Active site: {"description":"Proton donor/acceptor","evidences":[{"source":"UniProtKB","id":"O58403","evidenceCode":"ECO:0000250"},{"source":"HAMAP-Rule","id":"MF_00258","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 3 |
| Details | Binding site: {"evidences":[{"source":"UniProtKB","id":"P22634","evidenceCode":"ECO:0000250"},{"source":"HAMAP-Rule","id":"MF_00258","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 1 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00258","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"10331867","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1B74","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 1 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"10331867","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1B74","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1b73 |
| Chain | Residue | Details |
| A | SER8 | |
| A | ASP7 | |
| A | CYS178 | |
| A | CYS70 |
| site_id | MCSA1 |
| Number of Residues | 6 |
| Details | M-CSA 1 |
| Chain | Residue | Details |
| A | ASP7 | activator, electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor |
| A | SER8 | electrostatic stabiliser, hydrogen bond donor, increase basicity |
| A | CYS70 | activator, electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
| A | GLU147 | activator, electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, increase basicity, proton donor |
| A | CYS178 | activator, hydrogen bond acceptor, proton acceptor, proton donor |
| A | HIS180 | electrostatic stabiliser, hydrogen bond donor |
